eF-site ID 1bs0-A PDB Code 1bs0 Chain A click to enlarge Title PLP-DEPENDENT ACYL-COA SYNTHASE Classification TRANSFERASE Compound PROTEIN (8-AMINO-7-OXONANOATE SYNTHASE) Source Escherichia coli (strain K12) (BIOF_ECOLI) Sequence A:  SWQEKINAALDARRAADALRRRYPVAQGAGRWLVADDRQY LNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSG YSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMA KEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARL LASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWL MVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGVS GAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLA VIRSDEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQ PLIVGDNSRALQLAEKLRQQGCWVTAIRPPTVPAGTARLR LTLTAAHEMQDIDRLLEVLHGNG Description Functional site 1) chain A residue 236 type sequence K description PLP-BINDING LYSINE. source : CAT 2) chain A residue 107 type sequence S description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 3) chain A residue 108 type sequence G description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 4) chain A residue 109 type sequence F description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 5) chain A residue 236 type sequence K description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 6) chain A residue 265 type sequence S description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 7) chain A residue 266 type sequence T description BINDING SITE FOR RESIDUE SO4 A 400 source : AC1 8) chain A residue 147 type sequence L description BINDING SITE FOR RESIDUE SO4 A 401 source : AC2 9) chain A residue 148 type sequence R description BINDING SITE FOR RESIDUE SO4 A 401 source : AC2 10) chain A residue 149 type sequence R description BINDING SITE FOR RESIDUE SO4 A 401 source : AC2 11) chain A residue 22 type sequence R description BINDING SITE FOR RESIDUE SO4 A 403 source : AC3 12) chain A residue 23 type sequence R description BINDING SITE FOR RESIDUE SO4 A 403 source : AC3 13) chain A residue 101 type sequence R description BINDING SITE FOR RESIDUE SO4 A 403 source : AC3 14) chain A residue 256 type sequence L description BINDING SITE FOR RESIDUE SO4 A 403 source : AC3 15) chain A residue 336 type sequence E description BINDING SITE FOR RESIDUE SO4 A 403 source : AC3 16) chain A residue 47 type catalytic sequence N description 430 source MCSA : MCSA1 17) chain A residue 133 type catalytic sequence H description 430 source MCSA : MCSA1 18) chain A residue 175 type catalytic sequence E description 430 source MCSA : MCSA1 19) chain A residue 179 type catalytic sequence S description 430 source MCSA : MCSA1 20) chain A residue 204 type catalytic sequence D description 430 source MCSA : MCSA1 21) chain A residue 207 type catalytic sequence H description 430 source MCSA : MCSA1 22) chain A residue 236 type catalytic sequence K description 430 source MCSA : MCSA1 23) chain A residue 236 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10642176, ECO:0000269|PubMed:16557306 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 233-242 type prosite sequence TFGKGFGVSG description AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFGKGFGVSG source prosite : PS00599 25) chain A residue 21 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10642176 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 133 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10642176 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 233 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10642176 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 352 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10642176 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 108 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10642176, ECO:0000269|PubMed:16557306 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 179 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10642176, ECO:0000269|PubMed:16557306 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 207 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10642176, ECO:0000269|PubMed:16557306 source Swiss-Prot : SWS_FT_FI2

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